BMRB Entry 51012

Name: Backbone resonance assignments of KRAS Q61H mutant bound to GDP
Published: 2021-11-21

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51012

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Backbone resonance assignments of KRAS Q61H mutant bound to GDP

Deposition date:

2021-07-08

Original release date:

2021-11-21

Authors:

Huang, Qiwei; Kang, Congbao

Citation:

Citation: Huang, Qiwei; Ng, Elizabeth Yihui; Li, Qingxin; Kang, CongBao. "1H, 15N and 13C resonance assignments of the Q61H mutant of human KRAS bound to GDP" Biomol. NMR Assignments 16, 51-56 (2022).
PubMed: 34787842

Assembly members:

Assembly members:
entity_1, polymer, 172 residues, Formula weight is not available
entity_GDP, non-polymer, 443.201 Da.
entity_MG, non-polymer, 24.305 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMTEYKLVVVGAGGVGKS ALTIQLIQNHFVDEYDPTIE DSYRKQVVIDGETCLLDILD TAGHEEYSAMRDQYMRTGEG FLCVFAINNTKSFEDIHHYR EQIKRVKDSEDVPMVLVGNK CDLPSRTVDTKQAQDLARSY GIPFIETSAKTRQGVDDAFY TLVREIRKHKEK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	485
15N chemical shifts	164
1H chemical shifts	650

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	KRAS	1
2	GDP	2
3	Mg ion	3

Entities:

Entity 1, KRAS 172 residues - Formula weight is not available

1

GLY

SER

HIS

MET

THR

GLU

TYR

LYS

LEU

VAL

2

VAL

GLY

ALA

GLY

VAL

GLY

LYS

SER

3

ALA

LEU

THR

ILE

GLN

LEU

ILE

GLN

ASN

HIS

4

PHE

VAL

ASP

GLU

TYR

ASP

PRO

THR

ILE

GLU

5

ASP

SER

TYR

ARG

LYS

GLN

VAL

ILE

ASP

6

GLY

GLU

THR

CYS

LEU

ASP

ILE

LEU

ASP

7

THR

ALA

GLY

HIS

GLU

TYR

SER

ALA

MET

8

ARG

ASP

GLN

TYR

MET

ARG

THR

GLY

GLU

GLY

9

PHE

LEU

CYS

VAL

PHE

ALA

ILE

ASN

THR

10

LYS

SER

PHE

GLU

ASP

ILE

HIS

TYR

ARG

11

GLU

GLN

ILE

LYS

ARG

VAL

LYS

ASP

SER

GLU

12

ASP

VAL

PRO

MET

VAL

LEU

VAL

GLY

ASN

LYS

13

CYS

ASP

LEU

PRO

SER

ARG

THR

VAL

ASP

THR

14

LYS

GLN

ALA

GLN

ASP

LEU

ALA

ARG

SER

TYR

15

GLY

ILE

PRO

PHE

ILE

GLU

THR

SER

ALA

LYS

16

THR

ARG

GLN

GLY

VAL

ASP

ALA

PHE

TYR

17

THR

LEU

VAL

ARG

GLU

ILE

ARG

LYS

HIS

LYS

18

GLU

LYS

Entity 2, GDP - C10 H15 N5 O11 P2 - 443.201 Da.

1

GDP

Entity 3, Mg ion - Mg - 24.305 Da.

1

MG

Samples:

sample_1: KRAS Q61H, [U-100% 13C; U-100% 15N], 0.9 mM; KRAS Q61H-2, [U-100% 15N], 0.9 mM; HEPES 20 mM; NaCl 150 mM; GDP 5 mM; MgCl2 4 mM

sample_conditions_1: ionic strength: 0.170 M; pH: 7.3; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1 - collection

NMRPipe - processing

NMRView - chemical shift assignment

NMR spectrometers:

Bruker Avance 700 MHz
Bruker Avance 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks